Molecular cloning, characterization and tissue expression of prophenoloxidase cDNA from the mosquito Armigeres subalbatus inoculated with Dirofilaria immitis microfilariae.
A cDNA encoding mosquito Armigeres subalbatus prophenol oxidase (As-pro-PO) was obtained by rapid amplification of cDNA ends-polymerase chain reaction (RACE-PCR) after Dirofilaria immitis inoculation. The 2205 bp As-pro-PO cDNA contains a 32 bp 5'-noncoding region, a 2055 bp open reading frame (685 amino acids), and a 118 bp 3'-noncoding region. Hydrophobic signal peptide for the endoplasmic reticulum targeting is not found in the NH2-terminal region. Two potential copper-binding domains, amino acids 197-245 and 345-412, are highly homologous to those of the other insect pro-POs. A 2.2 kb As-pro-PO transcript was identified by Northern blot analysis using D. immitis microfilariae-inoculated A. subalbatus. Both in situ hybridization and Northern blot analysis demonstrated that As-pro-PO mRNA was synthesized in mosquito haemocytes but not in other tissues, i.e. fat bodies, midguts and ovaries, etc.
Cho
W L
WL
Department of Parasitology, National Yang-Ming University, Shih-pai, Taipei, Taiwan, ROC.
Liu
H S
HS
Lee
C H
CH
Kuo
C C
CC
Chang
T Y
TY
Liu
C T
CT
Chen
C C
CC
D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D015152:Blotting, Northern; D004156:Catechol Oxidase / Q000235:genetics*; D003001:Cloning, Molecular; D009033:Culicidae / Q000201:enzymology* / Q000235:genetics / Q000469:parasitology; D018076:DNA, Complementary; D004183:Dirofilaria immitis / Q000502:physiology*; D004285:Dogs; D004792:Enzyme Precursors / Q000235:genetics*; D005260:Female; D017403:In Situ Hybridization; D008969:Molecular Sequence Data; D017422:Sequence Analysis, DNA; D017386:Sequence Homology, Amino Acid
D018076:DNA, Complementary; D004792:Enzyme Precursors; C038451:pro-phenoloxidase; D004156:Catechol Oxidase